Molecular architecture of the yeast Mediator complex

By Philip J Robinson, Michael J Trnka, Riccardo Pellarin, Charles H Greenberg, David Bushnell1, Ralph Davis, Alma L Burlingame, Andrej Sali, Roger Kornberg1

1. Stanford University

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Published on

Type

journal-article

Author

Philip J Robinson and Michael J Trnka and Riccardo Pellarin and Charles H Greenberg and David A Bushnell and Ralph Davis and Alma L Burlingame and Andrej Sali and Roger D Kornberg

Citation

Robinson, P.J. et al., 2015. Molecular architecture of the yeast Mediator complex. eLife, 4. Available at: http://dx.doi.org/10.7554/elife.08719.

Abstract

The 21-subunit Mediator complex transduces regulatory information from enhancers to promoters, and performs an essential role in the initiation of transcription in all eukaryotes. Structural information on two-thirds of the complex has been limited to coarse subunit mapping onto 2-D images from electron micrographs. We have performed chemical cross-linking and mass spectrometry, and combined the results with information from X-ray crystallography, homology modeling, and cryo-electron microscopy by an integrative modeling approach to determine a 3-D model of the entire Mediator complex. The approach is validated by the use of X-ray crystal structures as internal controls and by consistency with previous results from electron microscopy and yeast two-hybrid screens. The model shows the locations and orientations of all Mediator subunits, as well as subunit interfaces and some secondary structural elements. Segments of 20–40 amino acid residues are placed with an average precision of 20 Å. The model reveals roles of individual subunits in the organization of the complex.

DOI

Funding

NSF-STC Biology with X-ray Lasers (NSF-1231306)